liu.seSearch for publications in DiVA
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • oxford
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Structural typing of systemic amyloidoses by luminescent-conjugated polymer spectroscopy.
Linköping University, Department of Physics, Chemistry and Biology, Organic Chemistry. Linköping University, The Institute of Technology.ORCID iD: 0000-0002-5582-140X
University Hospital of Zurich.
Linköping University, Department of Physics, Chemistry and Biology, Organic Chemistry. Linköping University, The Institute of Technology.
Show others and affiliations
2010 (English)In: The American journal of pathology, ISSN 1525-2191, Vol. 176, no 2, 563-574 p.Article in journal (Refereed) Published
Abstract [en]

Most systemic amyloidoses are progressive and lethal, and their therapy depends on the identification of the offending proteins. Here we report that luminescent-conjugated thiophene polymers (LCP) sensitively detect amyloid deposits. The heterodisperse polythiophene acetic acid derivatives, polythiophene acetic acid (PTAA) and trimeric PTAA, emitted yellow-red fluorescence on binding to amyloid deposits, whereas chemically homogeneous pentameric formic thiophene acetic acid emitted green-yellow fluorescence. The geometry of LCPs modulates the spectral composition of the emitted light, thereby reporting ligand-induced steric changes. Accordingly, a screen of PTAA-stained amyloid deposits in histological tissue arrays revealed striking spectral differences between specimens. Blinded cluster assignments of spectral profiles of tissue samples from 108 tissue samples derived from 96 patients identified three nonoverlapping classes, which were found to match AA, AL, and ATTR immunotyping. We conclude that LCP spectroscopy is a sensitive and powerful tool for identifying and characterizing amyloid deposits.

Place, publisher, year, edition, pages
2010. Vol. 176, no 2, 563-574 p.
National Category
Natural Sciences
Identifiers
URN: urn:nbn:se:liu:diva-54046DOI: 10.2353/ajpath.2010.080797ISI: 000274111400008PubMedID: 20035056OAI: oai:DiVA.org:liu-54046DiVA: diva2:298015
Available from: 2010-02-19 Created: 2010-02-19 Last updated: 2014-04-08

Open Access in DiVA

No full text

Other links

Publisher's full textPubMed

Authority records BETA

Nilsson, PeterÅslund, AndreasKonradsson, Peter

Search in DiVA

By author/editor
Nilsson, PeterÅslund, AndreasKonradsson, Peter
By organisation
Organic ChemistryThe Institute of Technology
Natural Sciences

Search outside of DiVA

GoogleGoogle Scholar

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 116 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • oxford
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf